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Conserved domains on  [gi|1188118583|ref|XP_020781814|]
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proteasome subunit beta type-7 [Boleophthalmus pectinirostris]

Protein Classification

proteasome subunit beta( domain architecture ID 10132940)

proteasome subunit beta is a non-catalytic component of the proteasome which degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus; belongs to the N-terminal nucleophile (Ntn)-hydrolase superfamily

CATH:  3.60.20.10
Gene Ontology:  GO:0043161|GO:0010498|GO:0005839
MEROPS:  T01
PubMed:  7682410|8882582|1317508|7697118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 44-232 1.46e-145

proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


:

Pssm-ID: 239732  Cd Length: 189  Bit Score: 405.43  E-value: 1.46e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  44 TTICGVVFKGGVVLGADTRATEGMVVADKNCSKIHYISPNIYCCGAGTAADTEMTTQLISSNLELHSLSTGRLPRVATAN 123
Cdd:cd03763     1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 124 RMLKQMLFRYQGYIGAALVLGGVDCNGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYKPDMEEEEAKQLVRDAIA 203
Cdd:cd03763    81 TMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIE 160

                         170       180
                  ....*....|....*....|....*....
gi 1188118583 204 AGIFNDLGSGSNIDLCVISKSKVDYLRPH 232
Cdd:cd03763   161 AGIFNDLGSGSNVDLCVITKDGVEYLRNY 189
Pr_beta_C pfam12465
Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is ...
 235-271 3.60e-13

Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. The family is found in association with pfam00227. There is a conserved GTT sequence motif. There is a single completely conserved residue Y that may be functionally important. This family includes the C terminal of the beta-type subunits of the proteasome, a multimeric complex that degrades proteins into peptides as part of the MHC class I-mediated Ag-presenting pathway.


:

Pssm-ID: 463597  Cd Length: 36  Bit Score: 62.03  E-value: 3.60e-13
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1188118583 235 ANKKGVRTGDYKYKRGTTGVLTKVVaPLDLEVVEETI 271
Cdd:pfam12465   1 PNERGERQGSYKFKRGTTAVLSETV-PLKLEVVEEVV 36
 
Name Accession Description Interval E-value
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 44-232 1.46e-145

proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239732  Cd Length: 189  Bit Score: 405.43  E-value: 1.46e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  44 TTICGVVFKGGVVLGADTRATEGMVVADKNCSKIHYISPNIYCCGAGTAADTEMTTQLISSNLELHSLSTGRLPRVATAN 123
Cdd:cd03763     1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 124 RMLKQMLFRYQGYIGAALVLGGVDCNGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYKPDMEEEEAKQLVRDAIA 203
Cdd:cd03763    81 TMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIE 160

                         170       180
                  ....*....|....*....|....*....
gi 1188118583 204 AGIFNDLGSGSNIDLCVISKSKVDYLRPH 232
Cdd:cd03763   161 AGIFNDLGSGSNVDLCVITKDGVEYLRNY 189
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 41-221 1.89e-66

Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologs vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria. The second is call beta-proteobacteria proteasome homolog (BPH).


Pssm-ID: 459721 [Multi-domain]  Cd Length: 188  Bit Score: 205.11  E-value: 1.89e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  41 KTGTTICGVVFKGGVVLGADTRATEG-MVVADKNCSKIHYISPNIYCCGAGTAADTEMTTQLISSNLELHSLSTGRLPRV 119
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGsKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 120 ----ATANRMLKQMLFRYQGYIGAALVLGGVDCNG-PHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYKPDMEEEEA 194
Cdd:pfam00227  82 elaaRIADLLQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEA 161

                         170       180
                  ....*....|....*....|....*..
gi 1188118583 195 KQLVRDAIAAGIFNDLGSGSNIDLCVI 221
Cdd:pfam00227 162 VELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 41-234 9.13e-47

20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 156.07  E-value: 9.13e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  41 KTGTTICGVVFKGGVVLGADTRATEGMVVADKNCSKIHYISPNIYCCGAGTAADTEMTTQLISSNLELHSLSTGRLPRVA 120
Cdd:COG0638    33 KRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 121 TANRMLKQMLF-----RYQGYiGAALVLGGVDCNGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYKPDMEEEEAK 195
Cdd:COG0638   113 GLAKLLSDLLQgytqyGVRPF-GVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAV 191

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1188118583 196 QLVRDAIAAGIFNDLGSGSNIDLCVISKSKVDYLrPHDE 234
Cdd:COG0638   192 ELALRALYSAAERDSASGDGIDVAVITEDGFREL-SEEE 229
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 43-226 2.47e-45

proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the archaeal proteasome beta subunit, homologous to both the alpha subunit and to the alpha and beta subunits of eukaryotic proteasome subunits. This family is universal in the first 29 complete archaeal genomes but occasionally is duplicated. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 274690  Cd Length: 185  Bit Score: 150.82  E-value: 2.47e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  43 GTTICGVVFKGGVVLGADTRATEGMVVADKNCSKIHYISPNIYCCGAGTAADTEMTTQLISSNLELHSLSTGRLPRVATA 122
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 123 NRMLKQMLF--RYQGYIgAALVLGGVDCNGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYKPDMEEEEAKQLVRD 200
Cdd:TIGR03634  81 ATLLSNILNsnRFFPFI-VQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVR 159

                         170       180
                  ....*....|....*....|....*.
gi 1188118583 201 AIAAGIFNDLGSGSNIDLCVISKSKV 226
Cdd:TIGR03634 160 AIKSAIERDVASGNGIDVAVITKDGV 185
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 43-218 3.70e-26

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 103.14  E-value: 3.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  43 GTTICGVVFKGGVVLGADTRATEGMVVADKNCSKIHYISPNIYCCGAGTAADTEMTTQLISSNLELHSLSTGRLPRVATA 122
Cdd:PTZ00488   39 GTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAA 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 123 NRMLKQMLFRYQGY-IGAALVLGGVDCNGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYKPDMEEEEAKQLVRDA 201
Cdd:PTZ00488  119 SKILANIVWNYKGMgLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRRA 198

                         170
                  ....*....|....*..
gi 1188118583 202 IAAGIFNDLGSGSNIDL 218
Cdd:PTZ00488  199 IYHATFRDAYSGGAINL 215
Pr_beta_C pfam12465
Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is ...
 235-271 3.60e-13

Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. The family is found in association with pfam00227. There is a conserved GTT sequence motif. There is a single completely conserved residue Y that may be functionally important. This family includes the C terminal of the beta-type subunits of the proteasome, a multimeric complex that degrades proteins into peptides as part of the MHC class I-mediated Ag-presenting pathway.


Pssm-ID: 463597  Cd Length: 36  Bit Score: 62.03  E-value: 3.60e-13
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1188118583 235 ANKKGVRTGDYKYKRGTTGVLTKVVaPLDLEVVEETI 271
Cdd:pfam12465   1 PNERGERQGSYKFKRGTTAVLSETV-PLKLEVVEEVV 36
 
Name Accession Description Interval E-value
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 44-232 1.46e-145

proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239732  Cd Length: 189  Bit Score: 405.43  E-value: 1.46e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  44 TTICGVVFKGGVVLGADTRATEGMVVADKNCSKIHYISPNIYCCGAGTAADTEMTTQLISSNLELHSLSTGRLPRVATAN 123
Cdd:cd03763     1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 124 RMLKQMLFRYQGYIGAALVLGGVDCNGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYKPDMEEEEAKQLVRDAIA 203
Cdd:cd03763    81 TMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIE 160

                         170       180
                  ....*....|....*....|....*....
gi 1188118583 204 AGIFNDLGSGSNIDLCVISKSKVDYLRPH 232
Cdd:cd03763   161 AGIFNDLGSGSNVDLCVITKDGVEYLRNY 189
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 44-230 7.21e-87

proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 238893  Cd Length: 189  Bit Score: 256.99  E-value: 7.21e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  44 TTICGVVFKGGVVLGADTRATEGMVVADKNCSKIHYISPNIYCCGAGTAADTEMTTQLISSNLELHSLSTGRLPRVATAN 123
Cdd:cd01912     1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 124 RMLKQMLFRYQGY-IGAALVLGGVDC-NGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYKPDMEEEEAKQLVRDA 201
Cdd:cd01912    81 NLLSNILYSYRGFpYYVSLIVGGVDKgGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKKA 160

                         170       180
                  ....*....|....*....|....*....
gi 1188118583 202 IAAGIFNDLGSGSNIDLCVISKSKVDYLR 230
Cdd:cd01912   161 IDSAIERDLSSGGGVDVAVITKDGVEELR 189
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 44-221 2.35e-69

proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta subunits and the prokaryotic protease hslV subunit. Proteasomes are large multimeric self-compartmentalizing proteases, involved in the clearance of misfolded proteins, the breakdown of regulatory proteins, and the processing of proteins such as the preparation of peptides for immune presentation. Two main proteasomal types are distinguished by their different tertiary structures: the eukaryotic/archeal 20S proteasome and the prokaryotic proteasome-like heat shock protein encoded by heat shock locus V, hslV. The proteasome core particle is a highly conserved cylindrical structure made up of non-identical subunits that have their active sites on the inner walls of a large central cavity. The proteasome subunits of bacteria, archaea, and eukaryotes all share a conserved Ntn (N terminal nucleophile) hydrolase fold and a catalytic mechanism involving an N-terminal nucleophilic threonine that is exposed by post-translational processing of an inactive propeptide.


Pssm-ID: 238887  Cd Length: 182  Bit Score: 212.36  E-value: 2.35e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  44 TTICGVVFKGGVVLGADTRATEGMVVADKNCSKIHYISPNIYCCGAGTAADTEMTTQLISSNLELHSLSTGRLPRVATAN 123
Cdd:cd01906     1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 124 RMLKQMLFRYQGY---IGAALVLGGVDC-NGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYKPDMEEEEAKQLVR 199
Cdd:cd01906    81 KLLANLLYEYTQSlrpLGVSLLVAGVDEeGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELAL 160

                         170       180
                  ....*....|....*....|..
gi 1188118583 200 DAIAAGIFNDLGSGSNIDLCVI 221
Cdd:cd01906   161 KALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 41-221 1.89e-66

Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologs vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria. The second is call beta-proteobacteria proteasome homolog (BPH).


Pssm-ID: 459721 [Multi-domain]  Cd Length: 188  Bit Score: 205.11  E-value: 1.89e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  41 KTGTTICGVVFKGGVVLGADTRATEG-MVVADKNCSKIHYISPNIYCCGAGTAADTEMTTQLISSNLELHSLSTGRLPRV 119
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGsKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 120 ----ATANRMLKQMLFRYQGYIGAALVLGGVDCNG-PHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYKPDMEEEEA 194
Cdd:pfam00227  82 elaaRIADLLQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEA 161

                         170       180
                  ....*....|....*....|....*..
gi 1188118583 195 KQLVRDAIAAGIFNDLGSGSNIDLCVI 221
Cdd:pfam00227 162 VELAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 44-227 4.54e-48

proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239731  Cd Length: 188  Bit Score: 158.16  E-value: 4.54e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  44 TTICGVVFKGGVVLGADTRATEGMVVADKNCSKIHYISPNIYCCGAGTAADTEMTTQLISSNLELHSLSTGRLPRVATAN 123
Cdd:cd03762     1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 124 RMLKQMLFRYQGYIGAALVLGGVDC-NGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYKPDMEEEEAKQLVRDAI 202
Cdd:cd03762    81 SLFKNLCYNYKEMLSAGIIVAGWDEqNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                         170       180
                  ....*....|....*....|....*
gi 1188118583 203 AAGIFNDLGSGSNIDLCVISKSKVD 227
Cdd:cd03762   161 SLAMSRDGSSGGVIRLVIITKDGVE 185
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 44-204 3.02e-47

The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are activated autocatalytically via an N-terminally lcated nucleophilic amino acid. N-terminal nucleophile (NTN-) hydrolase superfamily, which contains a four-layered alpha, beta, beta, alpha core structure. This family of hydrolases includes penicillin acylase, the 20S proteasome alpha and beta subunits, and glutamate synthase. The mechanism of activation of these proteins is conserved, although they differ in their substrate specificities. All known members catalyze the hydrolysis of amide bonds in either proteins or small molecules, and each one of them is synthesized as a preprotein. For each, an autocatalytic endoproteolytic process generates a new N-terminal residue. This mature N-terminal residue is central to catalysis and acts as both a polarizing base and a nucleophile during the reaction. The N-terminal amino group acts as the proton acceptor and activates either the nucleophilic hydroxyl in a Ser or Thr residue or the nucleophilic thiol in a Cys residue. The position of the N-terminal nucleophile in the active site and the mechanism of catalysis are conserved in this family, despite considerable variation in the protein sequences.


Pssm-ID: 238884 [Multi-domain]  Cd Length: 164  Bit Score: 155.25  E-value: 3.02e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  44 TTICGVVFKGGVVLGADTRATEGMVVADKNCSKIHYISPNIYCCGAGTAADTEMTTQLISSNLELHSLSTGRLPRVATAN 123
Cdd:cd01901     1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 124 RMLKQMLFRYQ--GYIGAALVLGGVDCNGPHLYSIYPHGSTDKLP-YVTMGSGSLAAMAVFEDRYKPDMEEEEAKQLVRD 200
Cdd:cd01901    81 KELAKLLQVYTqgRPFGVNLIVAGVDEGGGNLYYIDPSGPVIENPgAVATGSRSQRAKSLLEKLYKPDMTLEEAVELALK 160


                  ....
gi 1188118583 201 AIAA 204
Cdd:cd01901   161 ALKS 164
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 41-234 9.13e-47

20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 156.07  E-value: 9.13e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  41 KTGTTICGVVFKGGVVLGADTRATEGMVVADKNCSKIHYISPNIYCCGAGTAADTEMTTQLISSNLELHSLSTGRLPRVA 120
Cdd:COG0638    33 KRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 121 TANRMLKQMLF-----RYQGYiGAALVLGGVDCNGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYKPDMEEEEAK 195
Cdd:COG0638   113 GLAKLLSDLLQgytqyGVRPF-GVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAV 191

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1188118583 196 QLVRDAIAAGIFNDLGSGSNIDLCVISKSKVDYLrPHDE 234
Cdd:COG0638   192 ELALRALYSAAERDSASGDGIDVAVITEDGFREL-SEEE 229
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 44-224 9.63e-46

Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme for non-lysosomal protein degradation in both the cytosol and the nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are both members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239733  Cd Length: 188  Bit Score: 152.02  E-value: 9.63e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  44 TTICGVVFKGGVVLGADTRATEGMVVADKNCSKIHYISPNIYCCGAGTAADTEMTTQLISSNLELHSLSTGRLPRVATAN 123
Cdd:cd03764     1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 124 RMLKQMLF--RYQGYIgAALVLGGVDCNGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYKPDMEEEEAKQLVRDA 201
Cdd:cd03764    81 TLLSNILNssKYFPYI-VQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRA 159

                         170       180
                  ....*....|....*....|...
gi 1188118583 202 IAAGIFNDLGSGSNIDLCVISKS 224
Cdd:cd03764   160 IKSAIERDSASGDGIDVVVITKD 182
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 43-226 2.47e-45

proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the archaeal proteasome beta subunit, homologous to both the alpha subunit and to the alpha and beta subunits of eukaryotic proteasome subunits. This family is universal in the first 29 complete archaeal genomes but occasionally is duplicated. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 274690  Cd Length: 185  Bit Score: 150.82  E-value: 2.47e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  43 GTTICGVVFKGGVVLGADTRATEGMVVADKNCSKIHYISPNIYCCGAGTAADTEMTTQLISSNLELHSLSTGRLPRVATA 122
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 123 NRMLKQMLF--RYQGYIgAALVLGGVDCNGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYKPDMEEEEAKQLVRD 200
Cdd:TIGR03634  81 ATLLSNILNsnRFFPFI-VQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVR 159

                         170       180
                  ....*....|....*....|....*.
gi 1188118583 201 AIAAGIFNDLGSGSNIDLCVISKSKV 226
Cdd:TIGR03634 160 AIKSAIERDVASGNGIDVAVITKDGV 185
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 44-224 2.51e-32

proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239730  Cd Length: 188  Bit Score: 117.35  E-value: 2.51e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  44 TTICGVVFKGGVVLGADTRATEGMVVADKNCSKIHYISPNIYCCGAGTAADTEMTTQLISSNLELHSLSTGRLPRVATAN 123
Cdd:cd03761     1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 124 RMLKQMLFRYQGY-IGAALVLGGVDCNGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYKPDMEEEEAKQLVRDAI 202
Cdd:cd03761    81 KLLSNMLYQYKGMgLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAI 160

                         170       180
                  ....*....|....*....|..
gi 1188118583 203 AAGIFNDLGSGSNIDLCVISKS 224
Cdd:cd03761   161 YHATHRDAYSGGNVNLYHVRED 182
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 43-218 3.70e-26

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 103.14  E-value: 3.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  43 GTTICGVVFKGGVVLGADTRATEGMVVADKNCSKIHYISPNIYCCGAGTAADTEMTTQLISSNLELHSLSTGRLPRVATA 122
Cdd:PTZ00488   39 GTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAA 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 123 NRMLKQMLFRYQGY-IGAALVLGGVDCNGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYKPDMEEEEAKQLVRDA 201
Cdd:PTZ00488  119 SKILANIVWNYKGMgLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRRA 198

                         170
                  ....*....|....*..
gi 1188118583 202 IAAGIFNDLGSGSNIDL 218
Cdd:PTZ00488  199 IYHATFRDAYSGGAINL 215
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 39-222 3.07e-22

proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239725 [Multi-domain]  Cd Length: 211  Bit Score: 91.62  E-value: 3.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  39 ARKTGTTICGVVFKGGVVLGADTRATEGMVVADkNCSKIHYISPNIYCCGAGTAADTEMTTQLISSNLELHSLSTGRLPR 118
Cdd:cd03756    24 AVKRGTTALGIKCKEGVVLAVDKRITSKLVEPE-SIEKIYKIDDHVGAATSGLVADARVLIDRARVEAQIHRLTYGEPID 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 119 VATANRM---LKQMLFRYQGY--IGAALVLGGVDCNGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYKPDMEEEE 193
Cdd:cd03756   103 VEVLVKKicdLKQQYTQHGGVrpFGVALLIAGVDDGGPRLFETDPSGAYNEYKATAIGSGRQAVTEFLEKEYKEDMSLEE 182

                         170       180
                  ....*....|....*....|....*....
gi 1188118583 194 AKQLVRDAIAAGIfNDLGSGSNIDLCVIS 222
Cdd:cd03756   183 AIELALKALYAAL-EENETPENVEIAYVT 210
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 43-223 5.94e-17

proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239726  Cd Length: 212  Bit Score: 77.30  E-value: 5.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  43 GTTICgvvFKGG--VVLGADTRATEGMVVADKNCSKIHYISPNIYCCGAGTAADTEMTTQLISSNLELHSLSTGRLPRVA 120
Cdd:cd03757     9 GTVLA---IAGNdfAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 121 TANRMLKQML-----FRYQGYIgaalVLGGVDCNG-PHLYSIYPHGSTDKLPYVTMGSGSLAAMAV---FEDRYKPDMEE 191
Cdd:cd03757    86 AIAQLLSTILysrrfFPYYVFN----ILAGIDEEGkGVVYSYDPVGSYERETYSAGGSASSLIQPLldnQVGRKNQNNVE 161

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1188118583 192 ------EEAKQLVRDAIAAGIFNDLGSGSNIDLCVISK 223
Cdd:cd03757   162 rtplslEEAVSLVKDAFTSAAERDIYTGDSLEIVIITK 199
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
39-222 6.82e-17

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 77.57  E-value: 6.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  39 ARKTGTTICGVVFKGGVVLGADTRATEGMVVADKnCSKIHYISPNIYCCGAGTAADTEmttQLISsnlelhslstgRLPR 118
Cdd:PRK03996   32 AVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSS-IEKIFKIDDHIGAASAGLVADAR---VLID-----------RARV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 119 VATANRM-----------------LKQMLFRYQGY--IGAALVLGGVDCNGPHLYSIYPHGSTdkLPY--VTMGSGSLAA 177
Cdd:PRK03996   97 EAQINRLtygepigvetltkkicdHKQQYTQHGGVrpFGVALLIAGVDDGGPRLFETDPSGAY--LEYkaTAIGAGRDTV 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1188118583 178 MAVFEDRYKPDMEEEEAKQLVRDAIAAGIfNDLGSGSNIDLCVIS 222
Cdd:PRK03996  175 MEFLEKNYKEDLSLEEAIELALKALAKAN-EGKLDPENVEIAYID 218
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 45-203 8.56e-17

proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis.Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239727  Cd Length: 193  Bit Score: 76.47  E-value: 8.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  45 TICGVVFKGGVVLGADTRATEGMVVADKNCSKIHYISPNIYCCGAGTAADTEMTTQLISSNLELHSLSTGRLPRV-ATAN 123
Cdd:cd03758     3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPkAAAN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 124 RMLKQML--FRYQGYIGAALVLGGVD-CNGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYKPDMEEEEAKQLVRD 200
Cdd:cd03758    83 FTRRELAesLRSRTPYQVNLLLAGYDkVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALELMKK 162


                  ...
gi 1188118583 201 AIA 203
Cdd:cd03758   163 CIK 165
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 42-231 2.75e-16

proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis.Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239729  Cd Length: 197  Bit Score: 75.30  E-value: 2.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  42 TGTTICGVVFKGGVVLGADTRATEGMVVADKNCSKIHYISPNIYCCGAGTAAD----TEMTTQLISSNLEL---HSLST- 113
Cdd:cd03760     1 TGTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADfqylKRLLDQLVIDDECLddgHSLSPk 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 114 ---GRLPRVATANRMLKQMLFRyqgyigaALVLGGVDCNG-PHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRY--KP 187
Cdd:cd03760    81 eihSYLTRVLYNRRSKMNPLWN-------TLVVGGVDNEGePFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWekKP 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1188118583 188 DMEEEEAKQLVRDAIAAGIFNDLGSGSNIDLCVISKSKVDYLRP 231
Cdd:cd03760   154 DLTEEEARALIEECMKVLYYRDARSINKYQIAVVTKEGVEIEGP 197
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 39-221 1.86e-14

proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 different alpha and 10 different beta proteasome subunit genes while archaea have one of each.


Pssm-ID: 238892 [Multi-domain]  Cd Length: 209  Bit Score: 70.16  E-value: 1.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  39 ARKTGTTICGVVFKGGVVLGADTRATEGMVVADKNcSKIHYISPNIYCCGAGTAADTEMTTQ---LISSNlelHSLSTGR 115
Cdd:cd01911    23 AVKNGSTAVGIKGKDGVVLAVEKKVTSKLLDPSSV-EKIFKIDDHIGCAVAGLTADARVLVNrarVEAQN---YRYTYGE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 116 LPRVAT-ANRM--LKQMLFRYQGY--IGAALVLGGVDCN-GPHLYSIYPHGStdklpYVT-----MGSGSLAAMAVFEDR 184
Cdd:cd01911    99 PIPVEVlVKRIadLAQVYTQYGGVrpFGVSLLIAGYDEEgGPQLYQTDPSGT-----YFGykataIGKGSQEAKTFLEKR 173

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1188118583 185 YKPDMEEEEAKQLVRDAIAAGIFNDLgSGSNIDLCVI 221
Cdd:cd01911   174 YKKDLTLEEAIKLALKALKEVLEEDK-KAKNIEIAVV 209
Pr_beta_C pfam12465
Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is ...
 235-271 3.60e-13

Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. The family is found in association with pfam00227. There is a conserved GTT sequence motif. There is a single completely conserved residue Y that may be functionally important. This family includes the C terminal of the beta-type subunits of the proteasome, a multimeric complex that degrades proteins into peptides as part of the MHC class I-mediated Ag-presenting pathway.


Pssm-ID: 463597  Cd Length: 36  Bit Score: 62.03  E-value: 3.60e-13
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1188118583 235 ANKKGVRTGDYKYKRGTTGVLTKVVaPLDLEVVEETI 271
Cdd:pfam12465   1 PNERGERQGSYKFKRGTTAVLSETV-PLKLEVVEEVV 36
20S_bact_beta TIGR03690
proteasome, beta subunit, bacterial type; Members of this family are the beta subunit of the ...
 43-202 3.74e-12

proteasome, beta subunit, bacterial type; Members of this family are the beta subunit of the 20S proteasome as found in Actinobacteria such as Mycobacterium, Rhodococcus, and Streptomyces. In Streptomyces, maturation during proteasome assembly was shown to remove a 53-amino acid propeptide. Most of the length of the propeptide is not included in this model. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 163402 [Multi-domain]  Cd Length: 219  Bit Score: 63.96  E-value: 3.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  43 GTTICGVVFKGGVVLGADTRATEGMVVADKNCSKIhYISPNIYCCG-AGTAADTEMTTQLISSNLELHSLSTGR-LPRVA 120
Cdd:TIGR03690   2 GTTIVALTYPGGVLMAGDRRATQGNMIASRDVEKV-YPTDEYSAVGiAGTAGLAIELVRLFQVELEHYEKIEGVpLTLDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 121 TANRmLKQMLfryQGYIGAAL-------VLGGVDCNGPH--LYSIYPHGS-TDKLPYVTMGSGSLAAMAVFEDRYKPDME 190
Cdd:TIGR03690  81 KANR-LAAMV---RGNLPAAMqglavvpLLAGYDLDAGAgrIFSYDVTGGrYEERGYHAVGSGSVFAKGALKKLYSPDLD 156

                         170
                  ....*....|..
gi 1188118583 191 EEEAKQLVRDAI 202
Cdd:TIGR03690 157 EDDALRVAVEAL 168
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 42-226 6.02e-12

proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239728  Cd Length: 195  Bit Score: 63.03  E-value: 6.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  42 TGTTICGVVFKGGVVLGADTRATEGMVVADKNCSKIHYISPNIYCCGAGTAADTEMTTQLISSNLELHSLSTGRLPRVAT 121
Cdd:cd03759     2 NGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 122 ANRMLKQMLF--RYQGYIGAALVLGGVDCNGPHLYSIYPHGSTDKL-PYVTMGSGSLAAMAVFEDRYKPDMEEEEAKQLV 198
Cdd:cd03759    82 FSSLISSLLYekRFGPYFVEPVVAGLDPDGKPFICTMDLIGCPSIPsDFVVSGTASEQLYGMCESLWRPDMEPDELFETI 161

                         170       180
                  ....*....|....*....|....*...
gi 1188118583 199 RDAIAAGIFNDLGSGSNIDLCVISKSKV 226
Cdd:cd03759   162 SQALLSAVDRDALSGWGAVVYIITKDKV 189
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 39-198 1.20e-11

proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239722 [Multi-domain]  Cd Length: 213  Bit Score: 62.74  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  39 ARKTGTTICGVVFKGGVVLGADTRATEGMVVADkNCSKIHYISPNIYCCGAGTAADT----------------------- 95
Cdd:cd03753    23 AIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPS-SVEKIMEIDDHIGCAMSGLIADArtlidharveaqnhrftynepmt 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  96 -EMTTQLISsNLelhSLSTGRLprvatanRMLKQMLFRYqgyIGAALVLGGVDCNGPHLYSIYPHGSTDKLPYVTMGSGS 174
Cdd:cd03753   102 vESVTQAVS-DL---ALQFGEG-------DDGKKAMSRP---FGVALLIAGVDENGPQLFHTDPSGTFTRCDAKAIGSGS 167

                         170       180
                  ....*....|....*....|....
gi 1188118583 175 LAAMAVFEDRYKPDMEEEEAKQLV 198
Cdd:cd03753   168 EGAQSSLQEKYHKDMTLEEAEKLA 191
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 39-230 6.06e-10

proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239719 [Multi-domain]  Cd Length: 227  Bit Score: 58.10  E-value: 6.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  39 ARKTGTTICGVVFKGGVVLgADTRATEGMVVADKNCSKIHYISPNIYCCGAGTAADTEMTTQLISSNLELHSLSTGRLPR 118
Cdd:cd03750    23 AVSSGAPSVGIKAANGVVL-ATEKKVPSPLIDESSVHKVEQITPHIGMVYSGMGPDFRVLVKKARKIAQQYYLVYGEPIP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 119 VataNRMLKQMLFRYQGY--------IGAALVLGGVDCNGPHLYSIYPHGStdklpYVT-----MGSGSLAAMAVFEDRY 185
Cdd:cd03750   102 V---SQLVREIASVMQEYtqsggvrpFGVSLLIAGWDEGGPYLYQVDPSGS-----YFTwkataIGKNYSNAKTFLEKRY 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1188118583 186 KPDMEEEeakqlvrDAIAAGI------FNDLGSGSNIDLCVISKSKV----------DYLR 230
Cdd:cd03750   174 NEDLELE-------DAIHTAIltlkegFEGQMTEKNIEIGICGETKGfrlltpaeikDYLA 227
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 43-198 1.12e-07

proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239721 [Multi-domain]  Cd Length: 213  Bit Score: 51.19  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  43 GTTIcGVVFKGGVVLGADTRATEGMVVADKNCSKIHYISPNIYCCGAGTAADTEMTTQLISSNLELHSLSTGRLPRVATA 122
Cdd:cd03752    30 GTCL-GILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSDANILINYARLIAQRYLYSYQEPIPVEQL 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 123 NRML---KQMLFRYQGY--IGAALVLGGVDCN-GPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYKPDMEEEEAKQ 196
Cdd:cd03752   109 VQRLcdiKQGYTQYGGLrpFGVSFLYAGWDKHyGFQLYQSDPSGNYSGWKATAIGNNNQAAQSLLKQDYKDDMTLEEALA 188


                  ..
gi 1188118583 197 LV 198
Cdd:cd03752   189 LA 190
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 48-227 6.15e-07

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 49.47  E-value: 6.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  48 GVVFKGGVVLGADTRATEGMVVADKNCSKIHYISPNIYCCGAGTAADTEMTTQLISSNLELHSLSTGRLPRVataNRMLK 127
Cdd:PTZ00246   36 GILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLTADANILINQCRLYAQRYRYTYGEPQPV---EQLVV 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 128 QMLFRYQGY--------IGAALVLGGVDCN-GPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYKPDMEEEEAKQLV 198
Cdd:PTZ00246  113 QICDLKQSYtqfgglrpFGVSFLFAGYDENlGYQLYHTDPSGNYSGWKATAIGQNNQTAQSILKQEWKEDLTLEQGLLLA 192

                         170       180
                  ....*....|....*....|....*....
gi 1188118583 199 RDAIAAGIFNDLGSGSNIDLCVISKSKVD 227
Cdd:PTZ00246  193 AKVLTKSMDSTSPKADKIEVGILSHGETD 221
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 39-221 9.62e-07

proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239724 [Multi-domain]  Cd Length: 207  Bit Score: 48.51  E-value: 9.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  39 ARKTGTTICGVVFKGGVVLGADTRATEGMVvADKNCSKIHYISPNIYCCGAGTAADTEMttqLIS-SNLEL--HSLSTGR 115
Cdd:cd03755    23 AVRKGTTAVGVRGKDCVVLGVEKKSVAKLQ-DPRTVRKICMLDDHVCLAFAGLTADARV---LINrARLECqsHRLTVED 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 116 LPRVATANRMLKQMLFRY--QGYI---GAALVLGGVDCNG-PHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYKPDM 189
Cdd:cd03755    99 PVTVEYITRYIAGLQQRYtqSGGVrpfGISTLIVGFDPDGtPRLYQTDPSGTYSAWKANAIGRNSKTVREFLEKNYKEEM 178

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1188118583 190 EEEEAKQLVRDAIAAGIfnDLGSGsNIDLCVI 221
Cdd:cd03755   179 TRDDTIKLAIKALLEVV--QSGSK-NIELAVM 207
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 43-194 4.90e-06

proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239720 [Multi-domain]  Cd Length: 212  Bit Score: 46.50  E-value: 4.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  43 GTTIcGVVFKGGVVLGADTRATEGMVVADKNcSKIHYISPNIYCCGAGTAADTEmttQLIS--------------SNLEL 108
Cdd:cd03751    31 GTAI-GIRCKDGVVLAVEKLVTSKLYEPGSN-KRIFNVDRHIGIAVAGLLADGR---HLVSrareeaenyrdnygTPIPV 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 109 HSLSTgrlpRVAtanrMLKQMLFRYQGY--IGAALVLGGVDCNGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYK 186
Cdd:cd03751   106 KVLAD----RVA----MYMHAYTLYSSVrpFGCSVLLGGYDSDGPQLYMIEPSGVSYGYFGCAIGKGKQAAKTELEKLKF 177


                  ....*...
gi 1188118583 187 PDMEEEEA 194
Cdd:cd03751   178 SELTCREA 185
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 39-204 7.95e-05

proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239718 [Multi-domain]  Cd Length: 211  Bit Score: 42.66  E-value: 7.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583  39 ARKTGTTICGVVFKGGVVLGADTRATEGMVVADKncsKIHYISPNIYCCGAGTAADTEMTTQLISSNLELHSLSTGR-LP 117
Cdd:cd03749    23 AVKQGSATVGLKSKTHAVLVALKRATSELSSYQK---KIFKVDDHIGIAIAGLTADARVLSRYMRQECLNYRFVYDSpIP 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188118583 118 RVATANRMLKQMLFRYQGY----IGAALVLGGVDCNGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYK--PDMEE 191
Cdd:cd03749   100 VSRLVSKVAEKAQINTQRYgrrpYGVGLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARSQSARTYLERHFEefEDCSL 179

                         170
                  ....*....|...
gi 1188118583 192 EEakqLVRDAIAA 204
Cdd:cd03749   180 EE---LIKHALRA 189
protease_HslV cd01913
Protease HslV and the ATPase/chaperone HslU are part of an ATP-dependent proteolytic system ...
 44-120 5.53e-03

Protease HslV and the ATPase/chaperone HslU are part of an ATP-dependent proteolytic system that is the prokaryotic homolog of the proteasome. HslV is a dimer of hexamers (a dodecamer) that forms a central proteolytic chamber with active sites on the interior walls of the cavity. HslV shares significant sequence and structural similarity with the proteasomal beta-subunit and both are members of the Ntn-family of hydrolases. HslV has a nucleophilic threonine residue at its N-terminus that is exposed after processing of the propeptide and is directly involved in active site catalysis.


Pssm-ID: 238894  Cd Length: 171  Bit Score: 36.79  E-value: 5.53e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1188118583  44 TTICGVVFKGGVVLGADTRATEGMVVADKNCSKIHYISPNIYCCG-AGTAADTEMTTQLISSNLELHSlstGRLPRVA 120
Cdd:cd01913     1 TTILAVRKNGKVVIAGDGQVTLGNTVMKGNARKVRRLYNGKVIAGfAGSTADAFTLFERFEAKLEQYP---GNLLRAA 75
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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